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Protein

Fibrinogen alpha chain

Gene

FGA

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization. Was originally thought to be essential for platelet aggregation, based on in vitro studies using anticoagulated blood. However, subsequent studies have shown that it is not absolutely required for thrombus formation in vivo. Enhances expression of SELP in activated platelets via an ITGB3-dependent pathway. Maternal fibrinogen is essential for successful pregnancy. Fibrin deposition is also associated with infection, where it protects against IFNG-mediated hemorrhage. May also facilitate the immune response via both innate and T-cell mediated pathways.By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Adaptive immunity, Blood coagulation, Hemostasis, Immunity, Innate immunity

Names & Taxonomyi

Protein namesi
Recommended name:
Fibrinogen alpha chain
Cleaved into the following 2 chains:
Gene namesi
Name:FGA
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Protein family/group databases

Allergomei1112. Bos d Fibrin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 192 PublicationsAdd BLAST19
PeptideiPRO_000000900520 – 38Fibrinopeptide A2 PublicationsAdd BLAST19
ChainiPRO_000000900639 – 615Fibrinogen alpha chainAdd BLAST577

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi50InterchainBy similarity
Disulfide bondi58Interchain (with C-72 in beta chain)By similarity
Disulfide bondi67Interchain (with C-47 in gamma chain)By similarity
Disulfide bondi71Interchain (with C-83 in beta chain)By similarity
Disulfide bondi183Interchain (with C-163 in gamma chain)By similarity
Disulfide bondi187Interchain (with C-200 in beta chain)By similarity
Glycosylationi325O-linked (GalNAc...)By similarity1
Disulfide bondi455 ↔ 485Combined sources1 Publication

Post-translational modificationi

Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsilon-(gamma-glutamyl)lysine cross-linking between gamma chains (stronger) and between alpha chains (weaker) of different monomers.
Forms F13A-mediated cross-links between a glutamine and the epsilon-amino group of a lysine residue, forming fibronectin-fibrinogen heteropolymers.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei38 – 39Cleavage; by thrombin; to release fibrinopeptide A2

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP02672.
PeptideAtlasiP02672.
PRIDEiP02672.

Interactioni

Subunit structurei

Heterohexamer; disulfide linked. Contains 2 sets of 3 non-identical chains (alpha, beta and gamma). The 2 heterotrimers are in head to head conformation with the N-termini in a small central domain.1 Publication

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000002145.

Structurei

Secondary structure

1615
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi60 – 62Combined sources3
Beta strandi66 – 68Combined sources3
Helixi70 – 95Combined sources26
Beta strandi417 – 419Combined sources3
Beta strandi421 – 423Combined sources3
Beta strandi443 – 445Combined sources3
Beta strandi450 – 453Combined sources4
Turni454 – 456Combined sources3
Beta strandi457 – 459Combined sources3
Turni466 – 468Combined sources3
Beta strandi475 – 477Combined sources3
Beta strandi480 – 482Combined sources3
Beta strandi483 – 486Combined sources4
Beta strandi497 – 500Combined sources4
Beta strandi505 – 507Combined sources3
Turni537 – 539Combined sources3
Turni555 – 558Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DEQX-ray3.50A/D/N/Q20-409[»]
1JY2X-ray1.40N/Q48-100[»]
1JY3X-ray1.60N/Q48-100[»]
2BAFNMR-A406-570[»]
2JORNMR-A438-515[»]
ProteinModelPortaliP02672.
SMRiP02672.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02672.

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili71 – 6021 PublicationAdd BLAST532

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi448 – 451Poly-Thr4
Compositional biasi537 – 542Poly-Ser6

Domaini

A long coiled coil structure formed by 3 polypeptide chains connects the central nodule to the C-terminal domains (distal nodules). The long C-terminal ends of the alpha chains fold back, contributing a fourth strand to the coiled coil structure.1 Publication

Keywords - Domaini

Coiled coil, Signal

Phylogenomic databases

eggNOGiKOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
HOGENOMiHOG000285947.
HOVERGENiHBG005668.
InParanoidiP02672.
KOiK03903.

Family and domain databases

InterProiIPR012290. Fibrinogen_a/b/g_coil_dom.
IPR021996. Fibrinogen_aC.
[Graphical view]
PfamiPF08702. Fib_alpha. 1 hit.
PF12160. Fibrinogen_aC. 1 hit.
[Graphical view]
SMARTiSM01212. Fib_alpha. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P02672-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFSVRDLCLV LSLVGAIKTE DGSDPPSGDF LTEGGGVRGP RLVERQQSAC
60 70 80 90 100
KETGWPFCSD EDWNTKCPSG CRMKGLIDEV DQDFTSRINK LRDSLFNYQK
110 120 130 140 150
NSKDSNTLTK NIVELMRGDF AKANNNDNTF KQISEDLRSR IEILRRKVIE
160 170 180 190 200
QVQRIKVLQK NVRDQLVDMK RLEVDIDIKI RSCKGSCSRA LEHKVDLEDY
210 220 230 240 250
KNQQKQLEQV IAINLLPSRD IQYLPLIKMS TITGPVPREF KSQLQEAPLE
260 270 280 290 300
WKALLEMQQT KMVLETFGGD GHARGDSVSQ GTGLAPGSPR KPGTSSIGNV
310 320 330 340 350
NPGSYGPGSS GTWNPGRPEP GSAGTWNPGR PEPGSAGTWN PGRPEPGSAG
360 370 380 390 400
TWNPGRPEPG SAGTWNPGRP EPGSAGTWNT GSSGSSSFRP DSSGHGNIRP
410 420 430 440 450
SSPDWGTFRE EGSVSSGTKQ EFHTGKLVTT KGDKELLIDN EKVTSGHTTT
460 470 480 490 500
TRRSCSKVIT KTVTNADGRT ETTKEVVKSE DGSDCGDADF DWHHTFPSRG
510 520 530 540 550
NLDDFFHRDK DDFFTRSSHE FDGRTGLAPE FAALGESGSS SSKTSTHSKQ
560 570 580 590 600
FVSSSTTVNR GGSAIESKHF KMEDEAESLE DLGFKGAHGT QKGHTKARPA
610
RGIHTSPLGE PSLTP
Length:615
Mass (Da):67,012
Last modified:April 18, 2006 - v5
Checksum:iA79B48E292DF627B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti189R → K in AAC67562 (Ref. 2) Curated1
Sequence conflicti238 – 239RE → KK in AAC67562 (Ref. 2) Curated2
Sequence conflicti360 – 372Missing in AAC67562 (Ref. 2) CuratedAdd BLAST13
Sequence conflicti375A → G in AAC67562 (Ref. 2) Curated1
Sequence conflicti457 – 458KV → S no nucleotide entry (Ref. 3) Curated2
Sequence conflicti612S → T no nucleotide entry (Ref. 3) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC102564 mRNA. Translation: AAI02565.1.
AF095463 Genomic DNA. Translation: AAC67562.1.
PIRiA05294.
S69114.
RefSeqiNP_001028798.1. NM_001033626.1.
UniGeneiBt.17997.

Genome annotation databases

GeneIDi522039.
KEGGibta:522039.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC102564 mRNA. Translation: AAI02565.1.
AF095463 Genomic DNA. Translation: AAC67562.1.
PIRiA05294.
S69114.
RefSeqiNP_001028798.1. NM_001033626.1.
UniGeneiBt.17997.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DEQX-ray3.50A/D/N/Q20-409[»]
1JY2X-ray1.40N/Q48-100[»]
1JY3X-ray1.60N/Q48-100[»]
2BAFNMR-A406-570[»]
2JORNMR-A438-515[»]
ProteinModelPortaliP02672.
SMRiP02672.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000002145.

Protein family/group databases

Allergomei1112. Bos d Fibrin.

Proteomic databases

PaxDbiP02672.
PeptideAtlasiP02672.
PRIDEiP02672.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi522039.
KEGGibta:522039.

Organism-specific databases

CTDi2243.

Phylogenomic databases

eggNOGiKOG2579. Eukaryota.
ENOG410ZYS4. LUCA.
HOGENOMiHOG000285947.
HOVERGENiHBG005668.
InParanoidiP02672.
KOiK03903.

Miscellaneous databases

EvolutionaryTraceiP02672.

Family and domain databases

InterProiIPR012290. Fibrinogen_a/b/g_coil_dom.
IPR021996. Fibrinogen_aC.
[Graphical view]
PfamiPF08702. Fib_alpha. 1 hit.
PF12160. Fibrinogen_aC. 1 hit.
[Graphical view]
SMARTiSM01212. Fib_alpha. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFIBA_BOVIN
AccessioniPrimary (citable) accession number: P02672
Secondary accession number(s): O97642, Q3T049
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 18, 2006
Last modified: November 2, 2016
This is version 126 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.